ID Q12A23_POLSJ Unreviewed; 750 AA.
AC Q12A23;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=(P)ppGpp synthetase I (GTP pyrophosphokinase), SpoT/RelA {ECO:0000313|EMBL:ABE44619.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:ABE44619.1};
GN OrderedLocusNames=Bpro_2703 {ECO:0000313|EMBL:ABE44619.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE44619.1, ECO:0000313|Proteomes:UP000001983};
RN [1] {ECO:0000313|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
CC -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate)
CC is a mediator of the stringent response that coordinates a variety of
CC cellular activities in response to changes in nutritional abundance.
CC {ECO:0000256|RuleBase:RU003847}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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DR EMBL; CP000316; ABE44619.1; -; Genomic_DNA.
DR RefSeq; WP_011483617.1; NC_007948.1.
DR AlphaFoldDB; Q12A23; -.
DR STRING; 296591.Bpro_2703; -.
DR KEGG; pol:Bpro_2703; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_4; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000001983; Chromosome.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR CDD; cd04876; ACT_RelA-SpoT; 1.
DR CDD; cd05399; NT_Rel-Spo_like; 1.
DR CDD; cd01668; TGS_RSH; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR004811; RelA/Spo_fam.
DR InterPro; IPR007685; RelA_SpoT.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR033655; TGS_RelA/SpoT.
DR NCBIfam; TIGR00691; spoT_relA; 1.
DR PANTHER; PTHR21262:SF31; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 1.
DR PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR Pfam; PF13291; ACT_4; 1.
DR Pfam; PF13328; HD_4; 1.
DR Pfam; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 1.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001983};
KW Transferase {ECO:0000313|EMBL:ABE44619.1}.
FT DOMAIN 411..472
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 675..750
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 750 AA; 81701 MW; BBE26435A012BE76 CRC64;
MKSNVLGPDG PTAPQRPNAS IVTATADSPP DQPNALARAR AFAEPLIAGE TLDTGENILA
HADAVAAILK GIGGSEAMQA ATYLVHACQH LTKPQEVIAK AFGANYAALA IETTKLVHVQ
RQARTADAKA QLLDDPAAQT ENVRKMLLAF SRDLRVVMLR LASRLQTLRY YAATRQSAPL
ALAHESLHVF APLANRLGIW QIKWEMEDLA FRFLEPDTYK HTARLLDEKR VEREGFMESL
RAQLERELNQ NGIAALVQGR PKHIYSIVKK MRGKSLGFDQ VFDIRALRVI AADINGCYAA
LGFVHSRFTP VAGEFDDYIA KPKSNGYQSL HTVVRDAAGR AVEIQIRTQA MHDHAEHGVA
AHWAYKEAGT KGYSGVSASS EYDAKIAVLR QLLAWERDLS GPAAKQGLFE DRIYVLTPDA
AIVELPQGAT AVDFAYSVHT SLGHRCRGAR IDGAMVPLNT PLQNGQTVEV VTAKEGGPSR
DWLNSELGFL ASHRAKSKVR AWFNALAMEQ TVAKGREAVE KLLQREGKTA MKLDDLALQL
GFKTADDLFE VVGKDELSLR TIENMLRPPE PVLSQDDYVL AKKARQPDKS SQSGKGGKGS
VLVVGIDSLL TQLAKCCKPA PPDEILGFVT KGKGVSIHRS DCSNFRNMAS GSPDRVIEVQ
WSSSKTADGS VYPVDVAVEA ADRQGLLRDI SEVFAKEKMN VIGVQTQSVK DNRGGTAWMT
FTVEVAQSGR LNQVLGLVAD VPGVRSARRR
//
